Development of a Clickable Probe for Profiling of Protein Glutathionylation in the Central Cellular Metabolism of E. coli and Drosophila Protein glutathionylation is an important post-translational ...

The disulfide linkage between glutathione and protein is reversible, through the action of thiol-disulfide oxidoreductases. Glutathionylation substantially alters the functionality of enzymes ...

Together with its oxidized partner (GSSG), GSH maintains cellular redox homeostasis and regulates protein functions through S-glutathionylation. These important functions are dynamically regulated by ...

This realization has placed made glutaredoxin a focal point in advancing understanding of protein-S-glutathionylation as a regulatory mechanism akin to phosphorylation of proteins. We are employing a ...

This realization has placed made glutaredoxin a focal point in advancing understanding of protein-S-glutathionylation as a regulatory mechanism akin to phosphorylation of proteins. We are employing a ...

We are interested in interrogating redox-mediated biological processes, especially using a suite of chemical tools and methods that enable an understanding of protein cysteine oxidation at the ...

glutathionylation, and glycosylation) at the single-molecule level for protein chains over 1,200 residues long. These included modifications deep within the protein's sequence. Importantly ...

glutathionylation, and glycosylation). These included modifications deep within the protein’s sequence. Importantly, the method does not require the use of labels, enzymes, or additional reagents.

James Chun Yip Chan and colleagues at the National University of Singapore examined glutathionylation, a post-translational modification made to cysteine residues, in response to acetaminophen ...

Importantly, Dr. Madesh and colleagues found that S-glutathionylation of Cys-97 is reversible. "Reversible oxidation is essential to the regulation of protein function," Dr. Madesh explained.